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Structure of the connexin 26 gap junction channel at 3.5 Å resolution

Author

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  • Shoji Maeda

    (Institute for Protein Research, Osaka University, OLABB, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan)

  • So Nakagawa

    (Institute for Protein Research, Osaka University, OLABB, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan)

  • Michihiro Suga

    (Institute for Protein Research, Osaka University, OLABB, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan)

  • Eiki Yamashita

    (Institute for Protein Research, Osaka University, OLABB, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan)

  • Atsunori Oshima

    (Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan)

  • Yoshinori Fujiyoshi

    (Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan)

  • Tomitake Tsukihara

    (Institute for Protein Research, Osaka University, OLABB, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan
    Picobiology Institute, Graduate School of Life Science, University of Hyogo, Kamigohori, Akoh, Hyogo 678-1297, Japan)

Abstract

Gap junctions consist of arrays of intercellular channels between adjacent cells that permit the exchange of ions and small molecules. Here we report the crystal structure of the gap junction channel formed by human connexin 26 (Cx26, also known as GJB2) at 3.5 Å resolution, and discuss structural determinants of solute transport through the channel. The density map showed the two membrane-spanning hemichannels and the arrangement of the four transmembrane helices of the six protomers forming each hemichannel. The hemichannels feature a positively charged cytoplasmic entrance, a funnel, a negatively charged transmembrane pathway, and an extracellular cavity. The pore is narrowed at the funnel, which is formed by the six amino-terminal helices lining the wall of the channel, which thus determines the molecular size restriction at the channel entrance. The structure of the Cx26 gap junction channel also has implications for the gating of the channel by the transjunctional voltage.

Suggested Citation

  • Shoji Maeda & So Nakagawa & Michihiro Suga & Eiki Yamashita & Atsunori Oshima & Yoshinori Fujiyoshi & Tomitake Tsukihara, 2009. "Structure of the connexin 26 gap junction channel at 3.5 Å resolution," Nature, Nature, vol. 458(7238), pages 597-602, April.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7238:d:10.1038_nature07869
    DOI: 10.1038/nature07869
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    Cited by:

    1. Hyuk-Joon Lee & Hyung Jin Cha & Hyeongseop Jeong & Seu-Na Lee & Chang-Won Lee & Minsoo Kim & Jejoong Yoo & Jae-Sung Woo, 2023. "Conformational changes in the human Cx43/GJA1 gap junction channel visualized using cryo-EM," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Seu-Na Lee & Hwa-Jin Cho & Hyeongseop Jeong & Bumhan Ryu & Hyuk-Joon Lee & Minsoo Kim & Jejoong Yoo & Jae-Sung Woo & Hyung Ho Lee, 2023. "Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Zhihui He & Yonghui Zhao & Michael J. Rau & James A. J. Fitzpatrick & Rajan Sah & Hongzhen Hu & Peng Yuan, 2023. "Structural and functional analysis of human pannexin 2 channel," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    4. Hang Zhang & Shiyu Wang & Zhenzhen Zhang & Mengzhuo Hou & Chunyu Du & Zhenye Zhao & Horst Vogel & Zhifang Li & Kaige Yan & Xiaokang Zhang & Jianping Lu & Yujie Liang & Shuguang Yuan & Daping Wang & Hu, 2023. "Cryo-EM structure of human heptameric pannexin 2 channel," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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